ArticleBioanalysis2026
Vendor-specific HRP antibody conjugate differences lead to unexpected immunoassay reagent interactions.
Article in Bioanalysis, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimAn interaction observed in an anti-drug antibody (ADA) bridging ELISA between the drug and the anti-digoxin (aDIG) conjugated horseradish peroxidase (HRP) led to increased assay background across several commercial aDIG-HRP sources. Understanding the source of this interaction will help inform reagent qualities to be considered in production, evaluation, and selection for bioanalytical assays. METHODS AND MATERIALS: This work evaluates commercial sources of aDIG-HRP through bridging ELISA, binding ELISA, SPR, and chromatography to determine what characteristics of aDIG-HRP lead to the interaction observed in a bridging ELISA.
resultsThree of four commercial aDIG-HRP sources evaluated exhibit drug binding and size heterogeneity with large (>250 kDa) species. SE-UHPLC of one source localizes this binding capability to the >6 MDa species. Under typical HRP conjugation conditions, HRP can conjugate to itself, and these larger species can bind to drug.
conclusionThe conjugation of HRP to aDIG may lead to large species linked to HRP self-conjugation that can interfere with bioassays if not carefully controlled. Therefore, it is important to evaluate commercial reagents for consistency, availability, and critical quality when incorporating a new lot/vendor for better understanding of unexpected assay performance and effectively support reagent and assay life cycle management.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.